ペプシンで可溶化したホタテガイ外套膜由来コラーゲンの特性

日本食品科学工学会

日本食品科学工学会誌

Pepsin-solubilized collagen was prepared from scallop mantle. The scallop mantle pepsin solubilized collagen (SMPC) was subjected to analyses of amino acid composition, digestive pattern by protease, electron microscopic view of collagen fibers, and moisture absorption to evaluate its characteristics in comparison with bovine skin type I and bovine placental type V collagens. The amino acid composition of SMPC coincided with that of bovine type V collagen. The SDS-PAGE analysis showed that two α-chains were similar in molecular weight to those of bovine placental type V collagen. However, SMPC was more susceptible than bovine placental type V collagen to Staphylococcus aureus V8 protease digestion. The diameter of the SMPC gel fibril was about half of the bovine type I collagen gel fibril. Gel formation ability of the bovine type I collagen was higher than that of SMPC. SMPC showed a higher moisture absorption isotherm under high humidity than bovine skin type I collagen. Electron microscopic view of SMPC showed in part a sponge-like structure.